Residue-by-residue listing for refined_5 Page 1 ---------------------------------------- This listing highlights the residues in the structure which may need investigation. The ideal values and standard deviations against which the structure has been compared are shown in the following table: <------------------------------- I D E A L V A L U E S -------------------------------> Chi-1 dihedral Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality g(-) trans g(+) Chi-2 phi helix psi rt-hand lf-hand bond dihedral en. C-alpha ------------------------------------------------------------------------------------------ Ideal value 64.1 183.6 -66.7 177.4 -65.4 -65.3 -39.4 96.8 -85.8 2.0 180.0 -2.0 33.9 Standard deviation 15.7 16.8 15.0 18.5 11.2 11.9 11.3 14.8 10.7 .1 5.8 .8 3.5 ------------------------------------------------------------------------------------------ In the listing below, properties that deviate from these values are highlighted by asterisks and plus-signs. Each asterisk represents one standard deviation, and each plus-sign represents half a standard deviation. So, a highlight such as +***, indicates that the value of the parameter is between 3.5 and 4.0 standard deviations from the ideal value shown above. Where the deviation is greater than 4.5 standard deviations its numerical value is shown; for example, *5.5*. The final column gives the maximum deviation in each row, while the maximum column deviations are shown at the end of the listing. Also at the end are the keys to the codes used for the secondary structure and Ramachandran plot assignments. Full print-out. ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 1 GLY 1 - - - - - - - - - - - 180.5 - - - 2 HIS 2 B - 184.0 - - - - - - - - 180.2 - 34.5 - 3 HIS 3 B - 180.5 - - - - - - - - 177.4 -.5 33.2 - ** ** 4 HIS 4 b - 179.6 - - - - - - - - 179.0 -.6 33.7 - +* +* 5 HIS 5 B - 183.7 - - - - - - - - 180.9 - 34.2 - 6 HIS 6 B - 178.7 - - - - - - - - 178.3 - 35.4 - 7 HIS 7 B 64.9 - - - - - - - - - 176.8 - 32.9 - 8 LEU 8 B - - -61.1 178.2 - - - - - - 181.1 - 34.3 - 9 GLU 9 B 52.7 - - 178.1 - - - - - - 177.4 -.9 29.3 - * * * 10 CYS 10 B - 182.7 - - - - - - - - 182.2 -1.3 35.5 - * * 11 SER 11 b - 182.9 - - - - - - - - 170.4 -.7 33.4 - +* +* +* 12 SER 12 t A - - -56.1 - - - - - - - 175.7 - 34.8 - 13 ASP 13 T XX - 185.3 - - - - - - - - 180.4 - 30.7 - **** **** 14 SER 14 T a - 188.6 - - - - - - - - 178.6 -1.1 34.2 - * * 15 LEU 15 t b - - -69.1 - - - - - - - 177.4 -2.9 33.3 - * * 16 GLN 16 B - - -64.4 184.6 - - - - - - 175.6 -1.0 35.4 - * * 17 LEU 17 B - - -60.5 - - - - - - - 186.2 - 32.2 - * * Residue-by-residue listing for refined_5 Page 2 ---------------------------------------- ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 18 HIS 18 E B - - -58.4 - - - - - - - 176.7 -3.1 36.1 - * * 19 ASN 19 E B 60.8 - - - - - - - - - 185.6 - 31.2 - 20 VAL 20 E B - 181.5 - - - - - - - - 178.3 -2.3 35.8 - 21 PHE 21 E B - 179.9 - - - - - - - - 178.8 -3.1 35.2 - * * 22 VAL 22 E B 60.3 - - - - - - - - - 184.1 -3.3 32.2 - +* +* 23 TYR 23 A 57.6 - - - - - - - - - 181.1 - 32.2 - 24 GLY 24 t - - - - - - - - - - - 178.9 - - - 25 SER 25 T A 48.4 - - - - - - - - - 178.7 - 34.6 - 26 PHE 26 T b - - -65.6 - - - - - - - 184.1 - 35.1 - 27 GLN 27 t A 56.6 - - 177.8 - - - - - - 181.0 -1.0 32.9 - * * 28 ASP 28 h B - 178.6 - - - - - - - - 182.2 - 33.8 - 29 PRO 29 H - - - - - -65.2 -65.2 -25.0 - - - 183.8 - 38.7 - * * * 30 ASP 30 H A - 184.2 - - - -73.5 -30.0 - - - 174.9 - 31.7 - 31 VAL 31 H A - - -55.6 - - -72.4 -28.2 - - - 180.2 -.7 31.3 - +* +* 32 ILE 32 H A - - -59.0 - - -64.3 -40.4 - - - 175.9 -1.0 33.8 - * * 33 ASN 33 H A - - -67.0 - - -61.4 -30.2 - - - 182.5 -1.5 33.3 - 34 VAL 34 H A - 180.8 - - - -82.3 -50.9 - - - 184.4 -.8 33.8 - * * +* +* 35 MET 35 H A - 203.2 - - - -67.7 -35.6 - - - 179.1 -3.3 33.9 - * +* +* 36 LEU 36 h a - - -54.2 177.3 - - - - - - 186.4 -2.7 35.8 - * * 37 ASP 37 t ~b - 178.8 - - - - - - - - 186.9 -.9 36.3 - ** * +* ** 38 ARG 38 S B 53.2 - - 183.6 - - - - - - 179.1 - 35.7 - 39 THR 39 B - - -50.2 - - - - - - - 171.8 - 35.6 - * * * 40 PRO 40 - - - - - -65.8 - - - - - 179.2 - 39.3 - +* +* 41 GLU 41 E B - - -74.2 175.9 - - - - - - 185.5 -1.3 29.7 - * * 42 ILE 42 E B - - -52.5 178.5 - - - - - - 172.5 - 35.6 - * * 43 VAL 43 E B 62.9 - - - - - - - - - 177.7 -1.8 33.4 - 44 SER 44 E B - - -49.2 - - - - - - - 182.6 - 36.9 - * * 45 ALA 45 E B - - - - - - - - - - 179.5 -2.5 32.8 - 46 THR 46 E B - - -55.8 - - - - - - - 178.5 -2.8 35.6 - 47 LEU 47 E B - 176.0 - - - - - - - - 179.5 -3.5 35.3 - +* +* 48 PRO 48 E - - - - - -81.1 - - - - - 178.5 - 38.5 - * * * 49 GLY 49 e - - - - - - - - - - - 179.7 -2.5 - - 50 PHE 50 t B - - -70.2 - - - - - - - 182.1 -.7 33.4 - +* +* 51 GLN 51 E B - 178.5 - 174.6 - - - - - - 184.6 -2.8 33.7 - 52 ARG 52 E B - 207.7 - - - - - - - - 176.7 - 37.5 - * * * 53 PHE 53 e B - - -78.7 - - - - - - - 183.8 -2.6 32.9 - 54 ARG 54 B - 181.9 - - - - - - - - 185.8 -1.6 33.9 - Residue-by-residue listing for refined_5 Page 3 ---------------------------------------- ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 55 LEU 55 B - 189.5 - - - - - - - - 182.6 - 36.0 - 56 LYS 56 a 60.5 - - 178.3 - - - - - - 181.7 - 34.2 - 57 GLY 57 S - - - - - - - - - - - 181.8 - - - 58 ARG 58 S A 57.4 - - - - - - - - - 177.1 - 31.0 - 59 LEU 59 S B - 180.2 - - - - - - - - 189.6 - 31.9 - +* +* 60 TYR 60 B - - -50.1 - - - - - - - 171.7 - 37.1 - * * * 61 PRO 61 - - - - - -69.7 - - - - - 186.8 - 39.4 - * +* +* 62 CYS 62 e b 56.7 - - - - - - - - - 178.7 -1.2 34.5 - * * 63 ILE 63 E B - - -59.9 - - - - - - - 179.9 - 35.5 - 64 VAL 64 E B - - -59.4 - - - - - - - 178.8 -1.7 33.1 - 65 PRO 65 - - - - - -63.3 - - - - - 178.0 - 38.2 - * * 66 SER 66 t B - 181.7 - - - - - - - - 181.0 - 34.8 - 67 GLU 67 T A - - -58.0 173.5 - - - - - - 183.4 - 36.4 - 68 LYS 68 T A - - -71.8 - - - - - - - 182.5 - 34.1 - 69 GLY 69 e - - - - - - - - - - - 174.3 -1.2 - - * * 70 GLU 70 E B 58.0 - - - - - - - - - 182.2 - 31.9 - 71 VAL 71 E B - 183.4 - - - - - - - - 175.6 -2.7 35.4 - 72 HIS 72 E B - - -67.0 - - - - - - - 182.3 -.5 33.3 - ** ** 73 GLY 73 E - - - - - - - - - - - 183.7 -3.3 - - +* +* 74 LYS 74 E B - - -60.6 - - - - - - - 176.1 -1.5 34.8 - 75 VAL 75 E B - 168.1 - - - - - - - - 177.9 -2.9 34.1 - * * 76 LEU 76 E B - - -55.5 180.2 - - - - - - 178.9 -3.2 36.2 - +* +* 77 MET 77 E B 54.4 - - 180.3 - - - - - - 187.2 -3.5 32.0 - * +* +* 78 GLY 78 E - - - - - - - - - - - 179.4 -1.3 - - 79 VAL 79 E B 66.7 - - - - - - - - - 181.5 -2.1 32.5 - 80 THR 80 h B - - -40.5 - - - - - - - 178.9 - 37.0 - +* +* 81 SER 81 H A 47.9 - - - - -56.8 -34.9 - - - 178.6 - 34.7 - * * 82 ASP 82 H A - - -68.0 - - -66.0 -46.1 - - - 175.9 - 32.2 - 83 GLU 83 H A - - -57.2 - - -70.3 -31.0 - - - 176.2 - 33.2 - 84 LEU 84 H A - 175.2 - - - -58.8 -51.9 - - - 179.2 -2.5 36.0 - * * 85 GLU 85 H A 59.7 - - 179.5 - -68.6 -28.7 - - - 177.6 -2.8 32.1 - 86 ASN 86 H A - 182.4 - - - -65.7 -47.5 - - - 177.5 -1.5 35.5 - 87 LEU 87 H A - - -63.2 173.6 - -61.1 -46.4 - - - 179.8 -3.0 35.6 - * * 88 ASP 88 H A - 180.3 - - - -62.6 -29.7 - - - 177.9 -2.6 34.4 - 89 ALA 89 H A - - - - - -75.2 -40.5 - - - 182.0 -1.5 34.7 - 90 VAL 90 H A - 180.9 - - - -72.8 -49.3 - - - 178.9 -2.1 32.2 - 91 GLU 91 H A - - -58.7 - - -80.0 -27.8 - - - 191.7 -2.9 34.3 - * * ** * ** 92 GLY 92 h - - - - - - - - - - - 180.8 -1.1 - - * * 93 ASN 93 T A - - -83.3 - - - - - - - 180.2 - 29.2 - * * * Residue-by-residue listing for refined_5 Page 4 ---------------------------------------- ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 94 GLU 94 T A - - -62.1 180.8 - - - - - - 177.6 -1.3 31.2 - 95 TYR 95 t B - - -71.7 - - - - - - - 180.3 -1.5 33.1 - 96 GLU 96 E B - 176.8 - 173.9 - - - - - - 181.3 -2.7 34.3 - 97 ARG 97 E B - 171.9 - 174.9 - - - - - - 182.4 - 33.4 - 98 VAL 98 E B - - -62.4 - - - - - - - 183.0 -3.0 32.5 - * * 99 THR 99 E B 43.8 - - - - - - - - - 184.9 - 34.5 - * * 100 VAL 100 E B - - -64.2 - - - - - - - 177.1 -3.1 34.0 - * * 101 GLY 101 E - - - - - - - - - - - 181.7 - - - 102 ILE 102 E B 53.3 - - - - - - - - - 177.4 -3.4 33.0 - +* +* 103 VAL 103 E B - 182.9 - - - - - - - - 181.3 -2.6 33.7 - 104 ARG 104 E B - - -56.6 177.9 - - - - - - 179.6 -3.7 35.1 - ** ** 105 GLU 105 e A - - -59.9 175.2 - - - - - - 181.2 -2.8 35.3 - 106 ASP 106 T A - - -70.3 - - - - - - - 174.0 -.9 30.7 - * * * 107 ASN 107 t ~a 68.5 - - - - - - - - - 182.5 -.9 28.9 - ** * * ** 108 SER 108 S ~b - - -66.3 - - - - - - - 186.1 - 34.8 - ** * ** 109 GLU 109 e B - - -63.7 - - - - - - - 179.9 - 33.0 - 110 LYS 110 E B 61.0 - - 182.8 - - - - - - 184.7 - 32.8 - 111 MET 111 E B - - -66.2 179.8 - - - - - - 177.7 -3.6 34.8 - ** ** 112 ALA 112 E B - - - - - - - - - - 182.0 - 34.1 - 113 VAL 113 E B - - -62.4 - - - - - - - 172.6 -3.0 34.6 - * * * 114 LYS 114 E B - - -52.8 190.3 - - - - - - 181.1 -1.3 33.5 - * * 115 THR 115 E B - 189.0 - - - - - - - - 178.2 -2.7 34.4 - 116 TYR 116 E B - - -60.3 - - - - - - - 182.6 -.6 33.3 - +* +* 117 MET 117 E B - 178.9 - 175.4 - - - - - - 178.2 -3.3 34.9 - +* +* 118 TRP 118 B - 188.2 - - - - - - - - 188.1 -2.2 35.2 - * * 119 ILE 119 S A - - -53.0 - - - - - - - 178.8 - 32.6 - 120 ASN 120 t b - 178.4 - - - - - - - - 189.6 - 31.7 - +* +* 121 LYS 121 T A 51.7 - - 187.5 - - - - - - 174.3 -1.6 31.9 - 122 ALA 122 T a - - - - - - - - - - 178.8 - 33.2 - 123 ASP 123 t B - 179.6 - - - - - - - - 181.8 -1.3 34.4 - 124 PRO 124 S - - - - - -92.4 - - - - - 182.2 - 39.6 - ** +* ** 125 ASP 125 S a - 183.5 - - - - - - - - 182.8 - 34.8 - 126 MET 126 a 60.1 - - 181.1 - - - - - - 178.1 - 34.9 - 127 PHE 127 b - - -68.4 - - - - - - - 175.3 - 31.8 - 128 GLY 128 - - - - - - - - - - - 187.4 -1.4 - - * * 129 GLU 129 B 56.9 - - 181.9 - - - - - - 179.1 - 31.2 - 130 TRP 130 h B - 202.7 - - - - - - - - 188.2 - 36.5 - * * * 131 ASN 131 H a - - -64.5 - - -62.0 .2 - - - 175.2 - 30.6 - +*** +*** Residue-by-residue listing for refined_5 Page 5 ---------------------------------------- ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 132 PHE 132 H A - 165.9 - - - -69.2 -32.8 - - - 177.8 - 35.3 - * * 133 GLU 133 H A 51.3 - - - - -72.7 -33.7 - - - 172.2 -2.5 29.3 - * * * 134 GLU 134 H A - 177.6 - 183.6 - -63.6 -40.5 - - - 179.0 -.5 35.2 - ** ** 135 TRP 135 H A - 180.6 - - - -67.1 -41.8 - - - 178.3 -1.8 31.9 - 136 LYS 136 H A - 184.3 - 175.2 - -62.6 -33.5 - - - 174.6 -2.4 32.7 - 137 ARG 137 H A - 167.3 - - - -59.8 -50.3 - - - 182.6 -1.7 35.8 - 138 LEU 138 H A - - -56.8 178.0 - -74.3 -26.4 - - - 180.0 -2.1 35.1 - * * 139 HIS 139 H A - 179.9 - - - -83.7 -20.8 - - - 180.9 -2.5 34.7 - +* +* +* 140 LYS 140 H A - 188.2 - - - -62.0 -34.8 - - - 185.2 -1.4 36.7 - 141 LYS 141 H A - - -62.8 - - -53.9 -31.5 - - - 177.9 -.6 30.7 - +* +* 142 LYS 142 H A - 186.9 - 179.9 - -58.0 -46.2 - - - 183.5 -1.0 35.6 - * * 143 PHE 143 H A - 198.5 - - - -76.8 -33.5 - - - 181.1 -1.1 35.1 - * * 144 ILE 144 H A - - -60.0 - - -63.2 -34.6 - - - 177.9 -2.2 32.1 - 145 GLU 145 H A - - -60.6 182.8 - -56.8 -34.6 - - - 175.2 -2.1 33.0 - 146 THR 146 H A - - -63.8 - - -80.9 -47.2 - - - 188.7 -.8 35.6 - * * +* +* 147 PHE 147 H A - 212.5 - - - -70.9 -30.4 - - - 178.3 -2.9 32.7 - +* * +* 148 LYS 148 H A - 179.1 - 179.7 - -57.9 -40.1 - - - 180.0 -3.6 34.5 - ** ** 149 LYS 149 H A - - -56.9 177.6 - -64.2 -38.5 - - - 178.6 -.6 35.4 - +* +* 150 ILE 150 H A - - -58.2 176.6 - -68.4 -38.1 - - - 177.6 -1.1 34.4 - * * 151 MET 151 H A - - -58.9 179.5 - -63.6 -41.8 - - - 179.0 -2.4 35.2 - 152 GLU 152 H A - - -59.5 179.4 - -70.5 -33.9 - - - 176.3 -2.4 33.6 - 153 CYS 153 H A - 178.9 - - - -62.1 -49.8 - - - 177.4 -2.0 34.4 - 154 LYS 154 H A - - -60.4 181.5 - -70.5 -23.5 - - - 182.1 -2.7 35.6 - * * 155 LYS 155 h l - 190.3 - - - - - - - - 177.9 -1.2 30.2 - * * * 156 LYS 156 t b - - -62.0 179.8 - - - - - - 177.4 -1.4 34.6 - 157 PRO 157 - - - - - -69.1 - - - - - 181.0 - 38.8 - * * 158 GLN 158 B - - -63.5 182.4 - - - - - - 178.0 - 34.0 - 159 GLY 159 - - - - - - - - - - - 180.7 - - - 160 GLN 160 B - 181.7 - 180.0 - - - - - - 182.4 - 35.0 - 161 GLY 161 - - - - - - - - - - - 180.6 - - - 162 ASN 162 B 64.9 - - - - - - - - - 181.2 - 33.8 - 163 ASP 163 B 62.8 - - - - - - - - - 179.4 - 33.2 - 164 ASP 164 B - 179.0 - - - - - - - - 182.0 - 35.0 - 165 ILE 165 B 54.0 - - 177.7 - - - - - - 176.4 - 32.4 - 166 SER 166 B - 186.4 - - - - - - - - 183.1 -.6 34.2 - +* +* 167 HIS 167 B 66.0 - - - - - - - - - 179.1 -1.1 32.1 - * * 168 VAL 168 B - 182.9 - - - - - - - - 181.4 - 35.2 - 169 LEU 169 b - 188.9 - 174.0 - - - - - - 177.9 - 34.5 - 170 ARG 170 B 59.5 - - 180.1 - - - - - - 181.1 - 34.2 - Residue-by-residue listing for refined_5 Page 6 ---------------------------------------- ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 171 GLU 171 B - - -63.2 181.4 - - - - - - 178.9 - 33.6 - 172 ASP 172 B 61.3 - - - - - - - - - 177.0 - 35.2 - 173 GLN 173 - - 182.3 - 182.6 - - - - - - - - 33.8 - ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: **** * +* +* ** +* +*** ** ** +* **** ----------------------------------------------------------------------------------------------------------------------------------- Mean values: 57.9 183.1 -61.4 179.3 -72.4 -67.1 -36.0 - - - 180.1 -2.0 34.1 Standard deviations: 5.9 8.5 7.1 3.6 10.6 7.3 10.0 - - - 3.7 .9 2.0 Numbers of values: 31 58 61 46 7 42 42 0 0 0 172 98 161 0 KEY TO CODES: ------------ Regions of the Ramachandran plot Secondary structure (extended Kabsch/Sander) -------------------------------- -------------------------------------------- A - Core alpha B - residue in isolated beta-bridge a - Allowed alpha E - extended strand, participates in beta-ladder ~a - Generous alpha ** Generous G - 3-helix (3/10 helix) B - Core beta H - 4-helix (alpha-helix) b - Allowed beta I - 5-helix (pi-helix) ~b - Generous beta ** Generous S - bend L - Core left-handed alpha T - hydrogen-bonded turn l - Allowed left-handed alpha ~l - Generous left-handed alpha ** Generous e - extension of beta-strand p - Allowed epsilon g - extension of 3/10 helix ~p - Generous epsilon ** Generous h - extension of alpha-helix XX - Outside major areas **** Disallowed Residue-by-residue listing for refined_5 Page 7 ---------------------------------------- M A I N C H A I N B O N D L E N G T H S A N D B O N D A N G L E S ..................................... Small molecule data ......................................... <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N --------------------------------------------------------------------------------------------------- Any - 1.231 - - - - - - - - - - ( .020) Pro 1.341 - - - 1.466 122.60 116.90 - - 111.80 103.00 122.00 ( .016) ( .015) ( 5.00) ( 1.50) ( 2.50) ( 1.10) ( 1.40) Except Pro 1.329 - - - - - - - - - - 123.00 ( .014) ( 1.60) Gly - - 1.516 - 1.451 120.60 116.40 120.80 - 112.50 - - ( .018) ( .016) ( 1.70) ( 2.10) ( 2.10) ( 2.90) Except Gly - - 1.525 - - - - 120.80 - - - - ( .021) ( 1.70) Ala - - - 1.521 - - - - 110.50 - 110.40 - ( .033) ( 1.50) ( 1.50) Ile,Thr,Val - - - 1.540 - - - - 109.10 - 111.50 - ( .027) ( 2.20) ( 1.70) Except Gly,Pro - - - - 1.458 121.70 116.20 - - 111.20 - - ( .019) ( 1.80) ( 2.00) ( 2.80) The rest - - - 1.530 - - - - 110.10 - 110.50 - ( .020) ( 1.90) ( 1.70) Note. The table above shows the mean values obtained from small molecule data by Engh & Huber (1991). The values shown in brackets are standard deviations ................................................................................................................................... Residue ------------- <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> No. Type Seq Max Chain no. C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N dev ----------------------------------------------------------------------------------------------------------------------------------- 1 GLY 1 - 1.236 1.499 - 1.461 - 117.11 120.11 - 110.37 - 122.77 2 HIS 2 1.308 1.225 1.520 1.543 1.447 121.27 116.67 120.36 110.70 109.18 110.29 122.96 +* +* 3 HIS 3 1.308 1.230 1.516 1.546 1.445 121.18 115.87 121.00 110.96 110.33 111.57 123.11 * * 4 HIS 4 1.296 1.230 1.511 1.539 1.439 122.41 115.84 120.97 110.83 109.36 111.32 123.17 ** ** 5 HIS 5 1.295 1.232 1.514 1.540 1.436 122.27 115.67 120.78 111.16 108.42 110.60 123.48 ** * ** 6 HIS 6 1.305 1.222 1.506 1.546 1.447 122.70 117.27 120.01 109.64 108.69 110.25 122.72 +* +* 7 HIS 7 1.296 1.227 1.516 1.556 1.441 120.09 116.72 120.33 111.15 109.50 112.17 122.94 ** * ** 8 LEU 8 1.301 1.238 1.514 1.537 1.440 121.49 116.77 120.77 110.18 108.78 111.23 122.41 ** ** 9 GLU 9 1.305 1.239 1.515 1.536 1.435 120.37 114.19 122.43 113.28 112.57 113.41 123.32 +* * * +* +* +* 10 CYS 10 1.294 1.228 1.515 1.543 1.420 122.96 116.95 120.20 111.32 106.91 109.02 122.73 +** +* +* +** 11 SER 11 1.311 1.240 1.534 1.552 1.437 120.82 115.75 121.17 111.17 111.83 110.57 122.78 * * * * Residue-by-residue listing for refined_5 Page 8 ---------------------------------------- ................................................................................................................................... Residue ------------- <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> No. Type Seq Max Chain no. C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N dev ----------------------------------------------------------------------------------------------------------------------------------- 12 SER 12 1.312 1.234 1.532 1.531 1.445 121.75 113.44 122.34 110.77 106.86 110.14 124.22 * * +* +* 13 ASP 13 1.329 1.230 1.532 1.530 1.459 126.19 117.21 120.37 112.67 113.93 111.41 122.39 ** * ** 14 SER 14 1.306 1.238 1.529 1.546 1.441 121.02 115.52 121.91 111.81 109.03 109.66 122.56 +* +* 15 LEU 15 1.314 1.228 1.500 1.504 1.393 122.20 115.58 121.01 110.66 110.76 111.51 123.21 * * * *** *** 16 GLN 16 1.304 1.235 1.486 1.532 1.445 122.81 116.96 119.91 107.22 108.57 112.55 123.13 +* +* +* * +* 17 LEU 17 1.296 1.231 1.495 1.507 1.416 120.61 115.44 121.04 110.67 109.47 113.39 123.50 ** * * ** +* ** 18 HIS 18 1.281 1.239 1.492 1.527 1.431 122.53 116.07 120.36 108.88 109.82 109.62 123.53 *** +* * *** 19 ASN 19 1.301 1.236 1.525 1.539 1.428 121.33 115.17 121.66 113.38 110.66 111.75 123.16 ** +* +* ** 20 VAL 20 1.311 1.224 1.521 1.568 1.456 122.94 116.62 120.31 109.00 110.00 110.10 123.07 * * * 21 PHE 21 1.307 1.232 1.518 1.543 1.441 122.49 116.35 120.78 110.84 108.69 109.32 122.86 +* +* 22 VAL 22 1.304 1.237 1.522 1.561 1.432 121.02 115.84 120.98 111.34 109.64 113.05 123.18 +* * * +* 23 TYR 23 1.309 1.230 1.528 1.533 1.444 121.54 117.41 120.30 111.55 113.52 110.94 122.29 * * 24 GLY 24 1.319 1.230 1.505 - 1.452 118.93 116.09 120.72 - 113.14 - 123.19 25 SER 25 1.314 1.233 1.541 1.517 1.448 122.67 115.66 121.10 111.55 111.79 108.00 123.24 * * * 26 PHE 26 1.319 1.223 1.520 1.536 1.453 123.58 116.29 120.93 109.52 109.25 110.37 122.78 * * 27 GLN 27 1.309 1.233 1.521 1.528 1.457 120.83 116.54 120.61 110.56 112.38 111.32 122.84 * * 28 ASP 28 1.304 1.218 1.523 1.526 1.448 121.17 117.98 120.57 110.61 110.56 110.67 121.45 +* +* 29 PRO 29 1.335 1.226 1.529 1.526 1.467 122.66 117.57 120.79 110.00 113.39 103.47 121.60 30 ASP 30 1.313 1.230 1.522 1.520 1.448 119.80 116.88 120.70 112.11 110.99 111.90 122.39 * * * * 31 VAL 31 1.331 1.229 1.525 1.568 1.462 120.11 115.69 121.15 110.61 109.32 114.91 123.15 * ** ** 32 ILE 32 1.332 1.233 1.540 1.548 1.444 122.91 116.67 120.73 110.97 110.61 110.51 122.57 33 ASN 33 1.329 1.222 1.511 1.535 1.469 121.79 115.79 121.18 108.93 111.04 112.92 123.03 * * 34 VAL 34 1.300 1.228 1.519 1.557 1.450 121.76 115.73 121.03 109.79 110.25 111.93 123.21 ** ** 35 MET 35 1.326 1.231 1.538 1.551 1.448 122.11 116.61 120.86 112.21 110.16 109.25 122.47 * * * 36 LEU 36 1.326 1.234 1.503 1.536 1.453 121.27 113.92 121.32 107.59 109.83 111.15 124.66 * * * * * 37 ASP 37 1.332 1.230 1.510 1.540 1.466 125.53 114.66 121.88 107.31 107.28 111.27 123.42 ** * * ** 38 ARG 38 1.316 1.226 1.491 1.532 1.441 122.51 116.51 119.98 109.96 109.77 109.15 123.51 +* +* 39 THR 39 1.299 1.238 1.524 1.526 1.426 121.58 117.45 120.46 108.64 110.83 110.19 122.04 ** +* ** 40 PRO 40 1.335 1.241 1.516 1.534 1.453 122.64 116.80 120.14 109.78 109.29 103.74 123.02 * * Residue-by-residue listing for refined_5 Page 9 ---------------------------------------- ................................................................................................................................... Residue ------------- <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> No. Type Seq Max Chain no. C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N dev ----------------------------------------------------------------------------------------------------------------------------------- 41 GLU 41 1.301 1.224 1.483 1.490 1.438 120.99 113.94 122.16 112.62 112.98 113.12 123.89 +* ** ** * * * +* ** 42 ILE 42 1.266 1.240 1.513 1.556 1.431 121.86 115.67 121.02 108.33 110.45 110.95 123.30 *4.5* * *4.5* 43 VAL 43 1.291 1.247 1.518 1.565 1.433 122.10 116.69 120.22 110.38 107.81 112.93 123.05 +** * * +** 44 SER 44 1.299 1.237 1.515 1.516 1.427 121.62 117.94 119.76 109.59 106.41 108.25 122.26 ** +* +* * ** 45 ALA 45 1.300 1.227 1.505 1.503 1.432 119.51 114.58 121.83 110.64 113.32 111.00 123.59 ** * * ** 46 THR 46 1.289 1.220 1.520 1.536 1.421 123.39 115.97 120.49 109.52 109.50 109.80 123.53 +** +* +** 47 LEU 47 1.294 1.230 1.532 1.542 1.438 123.50 118.03 120.22 110.78 109.59 108.93 121.68 ** * * ** 48 PRO 48 1.339 1.245 1.528 1.530 1.450 122.17 116.07 120.72 110.73 111.90 103.39 123.19 * * 49 GLY 49 1.318 1.231 1.507 - 1.440 120.66 116.23 120.83 - 112.14 - 122.93 50 PHE 50 1.314 1.200 1.491 1.546 1.449 123.14 117.52 119.87 110.84 108.67 112.09 122.60 * +* +* +* 51 GLN 51 1.286 1.241 1.494 1.527 1.428 120.91 114.64 121.27 111.55 109.82 110.49 124.07 *** * +* *** 52 ARG 52 1.303 1.235 1.520 1.551 1.415 122.40 116.45 120.42 110.09 106.94 107.19 123.12 +* * ** +* +* ** 53 PHE 53 1.297 1.236 1.481 1.532 1.434 121.98 116.04 120.52 111.36 109.18 112.05 123.42 ** ** * ** 54 ARG 54 1.289 1.215 1.503 1.538 1.414 121.44 116.23 120.72 114.04 108.97 108.11 123.04 +** * ** ** * +** 55 LEU 55 1.298 1.234 1.519 1.533 1.428 121.39 117.53 119.72 111.48 108.02 107.57 122.73 ** +* * +* ** 56 LYS 56 1.314 1.242 1.529 1.546 1.458 121.25 115.85 121.01 110.53 111.01 110.21 123.12 * * 57 GLY 57 1.311 1.247 1.512 - 1.437 120.96 116.11 121.07 - 112.78 - 122.81 * * 58 ARG 58 1.314 1.230 1.528 1.561 1.452 121.59 115.95 121.04 113.21 112.00 111.67 123.01 * +* +* +* 59 LEU 59 1.306 1.235 1.533 1.545 1.439 122.30 116.41 120.20 113.28 109.33 111.40 123.39 +* * +* +* 60 TYR 60 1.314 1.234 1.522 1.537 1.445 122.97 117.51 120.29 107.60 110.68 109.04 122.19 * * * 61 PRO 61 1.346 1.241 1.538 1.547 1.459 122.71 116.43 120.57 109.90 109.83 103.43 122.99 62 CYS 62 1.310 1.252 1.547 1.527 1.449 122.40 115.15 121.39 110.86 113.36 108.44 123.45 * * * * * 63 ILE 63 1.341 1.248 1.518 1.568 1.460 124.17 116.68 120.27 108.24 108.12 111.75 123.04 * * * * 64 VAL 64 1.313 1.234 1.526 1.565 1.450 121.33 117.51 120.20 109.99 110.22 112.75 122.22 * * 65 PRO 65 1.337 1.235 1.542 1.536 1.467 123.15 115.85 121.11 110.55 113.40 103.65 123.04 66 SER 66 1.315 1.231 1.525 1.532 1.441 123.05 116.96 120.22 110.54 108.78 110.01 122.81 67 GLU 67 1.316 1.232 1.516 1.506 1.462 122.25 115.47 121.13 107.60 110.50 109.68 123.41 * * * 68 LYS 68 1.313 1.231 1.522 1.560 1.449 122.55 117.51 120.27 109.38 111.33 111.61 122.17 * +* +* 69 GLY 69 1.314 1.247 1.511 - 1.438 118.89 114.71 121.36 - 114.20 - 123.92 * * * Residue-by-residue listing for refined_5 Page 10 ---------------------------------------- ................................................................................................................................... Residue ------------- <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> No. Type Seq Max Chain no. C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N dev ----------------------------------------------------------------------------------------------------------------------------------- 70 GLU 70 1.311 1.231 1.524 1.559 1.438 124.67 117.04 120.43 111.36 108.59 113.79 122.52 * * * +* +* +* 71 VAL 71 1.304 1.216 1.508 1.561 1.448 121.50 116.72 120.57 108.10 109.68 111.62 122.70 +* +* 72 HIS 72 1.301 1.232 1.502 1.545 1.447 120.81 116.06 120.31 110.87 108.24 112.26 123.62 ** * * * ** 73 GLY 73 1.299 1.237 1.493 - 1.422 121.17 116.78 120.48 - 110.88 - 122.72 ** * +* ** 74 LYS 74 1.291 1.227 1.512 1.540 1.436 121.04 116.44 120.53 110.17 110.29 110.09 123.01 +** * +** 75 VAL 75 1.306 1.227 1.509 1.548 1.437 121.88 114.88 120.86 109.50 110.77 111.71 124.25 +* * +* 76 LEU 76 1.310 1.228 1.514 1.541 1.433 123.51 116.61 120.34 108.51 108.13 110.20 123.00 * * * * * 77 MET 77 1.298 1.217 1.500 1.535 1.452 122.19 117.17 120.55 112.25 109.84 112.02 122.27 ** * * ** 78 GLY 78 1.296 1.238 1.507 - 1.421 119.30 115.77 121.02 - 109.96 - 123.21 ** +* ** 79 VAL 79 1.331 1.244 1.524 1.583 1.441 121.15 116.34 120.73 111.42 109.01 112.94 122.88 +* * +* 80 THR 80 1.299 1.236 1.532 1.518 1.410 122.09 116.35 120.55 109.43 108.95 107.72 123.10 ** +** ** +** 81 SER 81 1.302 1.229 1.544 1.509 1.441 123.57 116.61 120.52 111.66 111.81 107.69 122.84 +* * * +* +* 82 ASP 82 1.335 1.220 1.518 1.535 1.469 121.91 117.50 120.38 110.58 111.71 112.49 122.12 * * 83 GLU 83 1.312 1.209 1.535 1.548 1.456 120.92 117.10 120.16 109.89 109.64 112.72 122.73 * * * * 84 LEU 84 1.340 1.236 1.524 1.540 1.480 122.34 115.50 121.20 107.96 109.97 110.33 123.28 * * * 85 GLU 85 1.327 1.217 1.519 1.540 1.447 121.98 115.56 120.85 112.07 110.33 111.85 123.59 * * 86 ASN 86 1.325 1.218 1.531 1.553 1.462 123.77 116.25 120.79 111.26 108.65 108.24 122.96 * * * * 87 LEU 87 1.319 1.236 1.513 1.538 1.470 123.03 114.48 121.53 108.92 108.98 110.27 123.95 88 ASP 88 1.320 1.212 1.527 1.529 1.454 123.56 116.09 121.21 111.01 111.15 109.21 122.70 * * 89 ALA 89 1.309 1.230 1.528 1.521 1.447 122.49 116.40 120.79 110.07 110.87 109.80 122.81 * * 90 VAL 90 1.322 1.236 1.554 1.565 1.465 122.23 116.88 120.66 111.10 112.26 111.91 122.45 * * 91 GLU 91 1.314 1.239 1.563 1.537 1.474 122.22 115.49 121.14 109.89 112.87 109.71 123.34 * +* +* 92 GLY 92 1.328 1.231 1.533 - 1.481 124.20 119.56 119.20 - 119.55 - 121.23 +* ** +* ** * ** 93 ASN 93 1.308 1.233 1.506 1.538 1.471 119.20 117.54 120.27 111.56 113.81 114.56 122.19 * * ** ** 94 GLU 94 1.310 1.223 1.525 1.533 1.454 119.84 116.49 120.62 112.59 112.80 111.47 122.88 * * * * 95 TYR 95 1.319 1.230 1.521 1.540 1.457 122.56 116.89 120.21 110.85 110.05 111.77 122.89 96 GLU 96 1.318 1.228 1.517 1.537 1.449 121.76 115.84 120.92 111.08 110.58 109.60 123.23 97 ARG 97 1.312 1.233 1.523 1.542 1.442 122.40 115.51 121.40 112.09 110.56 109.99 123.08 * * * 98 VAL 98 1.310 1.235 1.514 1.546 1.446 122.56 115.73 120.77 110.25 111.68 112.78 123.50 * * Residue-by-residue listing for refined_5 Page 11 ---------------------------------------- ................................................................................................................................... Residue ------------- <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> No. Type Seq Max Chain no. C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N dev ----------------------------------------------------------------------------------------------------------------------------------- 99 THR 99 1.302 1.230 1.531 1.536 1.435 123.29 116.66 120.63 111.40 110.94 109.02 122.70 +* * * * +* 100 VAL 100 1.326 1.234 1.537 1.555 1.478 121.71 115.79 121.21 108.36 112.90 111.89 123.00 * * 101 GLY 101 1.323 1.233 1.519 - 1.448 121.79 116.64 120.27 - 111.17 - 123.09 102 ILE 102 1.317 1.209 1.509 1.575 1.459 123.32 116.94 120.38 110.58 111.33 112.08 122.68 * * * 103 VAL 103 1.299 1.225 1.520 1.548 1.447 121.58 116.30 120.37 110.07 109.45 112.06 123.32 ** ** 104 ARG 104 1.312 1.233 1.515 1.531 1.449 122.79 115.68 120.80 108.98 110.24 110.70 123.50 * * 105 GLU 105 1.307 1.227 1.512 1.522 1.448 122.94 116.29 120.70 108.94 110.00 110.39 123.00 +* +* 106 ASP 106 1.330 1.230 1.510 1.536 1.452 121.02 117.07 120.33 111.75 112.48 113.20 122.60 +* +* 107 ASN 107 1.323 1.224 1.537 1.577 1.446 120.18 117.49 119.02 114.00 111.02 114.17 123.34 ** * ** ** ** 108 SER 108 1.342 1.234 1.539 1.557 1.491 125.29 117.21 120.33 106.77 111.16 112.88 122.45 * +* +* +* * +* 109 GLU 109 1.324 1.224 1.502 1.511 1.457 121.19 115.55 121.07 110.65 113.15 110.81 123.37 * * 110 LYS 110 1.304 1.234 1.521 1.532 1.433 121.76 115.86 120.97 111.71 110.18 111.32 123.16 +* * +* 111 MET 111 1.296 1.218 1.484 1.512 1.451 123.33 114.37 121.62 107.48 112.21 111.92 124.01 ** +* * ** 112 ALA 112 1.280 1.240 1.520 1.513 1.438 122.75 116.06 120.71 110.39 109.37 110.71 123.24 +*** * +*** 113 VAL 113 1.311 1.233 1.505 1.558 1.458 123.36 116.45 120.77 107.36 109.68 113.37 122.69 * * * 114 LYS 114 1.291 1.222 1.516 1.522 1.428 120.56 117.58 119.81 111.39 108.22 111.17 122.59 +** +* * +** 115 THR 115 1.303 1.235 1.517 1.568 1.450 121.19 116.04 120.74 109.11 109.15 112.26 123.22 +* * +* 116 TYR 116 1.299 1.233 1.506 1.519 1.427 122.23 115.01 121.31 112.14 109.44 110.36 123.65 ** +* * ** 117 MET 117 1.294 1.240 1.520 1.545 1.430 123.21 115.98 120.48 111.17 109.55 109.18 123.50 ** * ** 118 TRP 118 1.314 1.235 1.531 1.530 1.443 122.56 117.46 119.73 111.97 107.74 108.11 122.78 * * * * 119 ILE 119 1.330 1.240 1.528 1.581 1.469 119.93 116.38 120.94 108.51 111.27 114.60 122.62 +* +* +* 120 ASN 120 1.311 1.224 1.513 1.557 1.453 121.54 113.45 123.00 114.13 107.98 111.49 123.52 * * * * ** * ** 121 LYS 121 1.305 1.227 1.521 1.537 1.447 124.30 116.58 120.68 113.23 114.44 109.32 122.71 +* * +* * +* 122 ALA 122 1.308 1.235 1.528 1.525 1.446 121.56 115.62 121.20 111.38 109.33 111.12 123.18 +* +* 123 ASP 123 1.334 1.231 1.540 1.540 1.471 122.82 118.07 120.54 109.70 110.84 110.51 121.39 * * 124 PRO 124 1.341 1.239 1.548 1.523 1.456 122.44 117.18 120.66 110.20 113.65 101.81 122.16 * * * 125 ASP 125 1.310 1.238 1.527 1.531 1.460 121.39 116.00 120.93 110.42 110.84 109.37 123.00 * * 126 MET 126 1.329 1.232 1.543 1.530 1.482 123.87 117.91 119.87 108.87 113.71 109.62 122.22 * * * Residue-by-residue listing for refined_5 Page 12 ---------------------------------------- ................................................................................................................................... Residue ------------- <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> No. Type Seq Max Chain no. C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N dev ----------------------------------------------------------------------------------------------------------------------------------- 127 PHE 127 1.327 1.232 1.520 1.536 1.451 120.96 114.93 121.50 110.34 111.78 113.33 123.47 +* +* 128 GLY 128 1.295 1.243 1.491 - 1.421 122.42 117.20 119.90 - 108.32 - 122.89 ** * +* * * ** 129 GLU 129 1.296 1.238 1.495 1.531 1.428 120.19 114.06 121.92 112.09 113.10 112.03 124.01 ** * +* * * ** 130 TRP 130 1.291 1.230 1.508 1.530 1.411 123.19 117.94 118.96 111.32 104.40 107.94 123.09 +** ** * ** +* +** 131 ASN 131 1.317 1.239 1.537 1.534 1.485 122.39 116.67 120.64 111.36 115.25 112.21 122.66 * * * * 132 PHE 132 1.311 1.232 1.541 1.518 1.400 123.87 116.71 120.84 112.64 109.66 106.92 122.43 * *** * * ** *** 133 GLU 133 1.338 1.234 1.520 1.553 1.458 120.77 114.56 121.53 114.69 111.29 112.61 123.92 * ** * ** 134 GLU 134 1.304 1.232 1.511 1.530 1.459 123.53 115.85 121.26 109.33 109.24 110.38 122.89 +* * +* 135 TRP 135 1.316 1.216 1.508 1.529 1.424 120.35 116.72 120.22 111.45 110.44 112.74 123.03 +* * +* 136 LYS 136 1.325 1.209 1.524 1.529 1.451 120.87 115.83 120.79 111.09 110.17 111.96 123.37 * * 137 ARG 137 1.316 1.226 1.539 1.530 1.457 123.13 115.94 121.46 109.48 110.87 108.69 122.60 * * 138 LEU 138 1.304 1.245 1.531 1.519 1.456 122.35 114.93 121.80 110.40 110.91 108.76 123.26 +* * +* 139 HIS 139 1.299 1.234 1.537 1.543 1.464 123.44 115.14 121.29 110.81 110.29 109.28 123.57 ** ** 140 LYS 140 1.314 1.235 1.524 1.539 1.454 124.41 115.33 120.99 109.01 110.00 108.33 123.65 * +* * +* 141 LYS 141 1.331 1.234 1.529 1.530 1.460 123.34 117.82 119.36 111.53 114.73 112.20 122.82 * * 142 LYS 142 1.338 1.228 1.513 1.536 1.468 121.06 114.71 121.91 107.62 109.01 111.51 123.37 * * 143 PHE 143 1.303 1.232 1.526 1.524 1.422 122.17 115.49 121.11 110.94 109.39 108.99 123.39 +* +* +* 144 ILE 144 1.325 1.203 1.526 1.561 1.457 122.59 118.17 119.42 110.93 112.13 112.40 122.38 * * 145 GLU 145 1.334 1.227 1.542 1.532 1.481 120.63 115.43 121.51 110.67 110.58 111.53 123.05 * * 146 THR 146 1.313 1.233 1.530 1.548 1.438 122.63 115.50 121.43 109.22 110.70 109.71 123.02 * * * * 147 PHE 147 1.314 1.220 1.529 1.523 1.437 121.82 116.87 120.22 111.70 112.38 110.51 122.92 * * * 148 LYS 148 1.324 1.225 1.521 1.538 1.466 123.18 115.98 120.60 110.30 110.33 110.06 123.35 149 LYS 149 1.328 1.230 1.523 1.530 1.458 122.35 114.80 121.57 109.41 108.95 109.96 123.60 150 ILE 150 1.320 1.234 1.542 1.556 1.449 123.27 116.05 121.07 110.64 109.79 110.25 122.85 151 MET 151 1.329 1.226 1.516 1.531 1.469 122.43 115.82 120.89 107.80 109.73 111.69 123.28 * * 152 GLU 152 1.324 1.233 1.526 1.524 1.452 122.20 115.73 120.68 110.81 110.39 110.73 123.59 153 CYS 153 1.325 1.239 1.535 1.541 1.456 123.10 116.19 120.92 110.90 110.21 109.75 122.88 154 LYS 154 1.329 1.234 1.513 1.511 1.462 122.11 114.27 121.25 108.56 110.35 109.93 124.48 155 LYS 155 1.318 1.227 1.524 1.572 1.443 125.35 114.24 122.13 115.11 109.31 112.13 123.32 ** ** +** +** 156 LYS 156 1.314 1.250 1.521 1.540 1.450 123.31 117.53 120.43 108.64 109.21 112.01 121.95 * * 157 PRO 157 1.338 1.236 1.527 1.540 1.467 122.62 116.99 120.49 110.35 110.63 103.61 122.51 Residue-by-residue listing for refined_5 Page 13 ---------------------------------------- ................................................................................................................................... Residue ------------- <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> No. Type Seq Max Chain no. C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N dev ----------------------------------------------------------------------------------------------------------------------------------- 158 GLN 158 1.308 1.241 1.502 1.519 1.448 121.20 115.82 120.56 109.73 111.23 111.13 123.62 +* * +* 159 GLY 159 1.310 1.243 1.506 - 1.431 121.27 116.29 120.47 - 111.08 - 123.25 * * * 160 GLN 160 1.298 1.238 1.512 1.531 1.437 122.75 116.49 119.71 110.68 108.04 109.85 123.79 ** * * ** 161 GLY 161 1.327 1.233 1.509 - 1.448 121.81 116.17 120.93 - 112.53 - 122.88 162 ASN 162 1.304 1.238 1.503 1.548 1.444 121.90 116.52 120.40 110.51 109.16 111.57 123.07 +* * +* 163 ASP 163 1.301 1.243 1.506 1.544 1.446 121.21 115.19 120.98 110.26 110.84 112.07 123.82 +* +* 164 ASP 164 1.302 1.231 1.515 1.529 1.443 123.12 117.22 120.24 110.31 108.99 109.81 122.52 +* +* 165 ILE 165 1.309 1.233 1.526 1.557 1.450 121.04 116.37 121.16 110.39 112.74 112.38 122.47 * * 166 SER 166 1.309 1.239 1.520 1.541 1.438 120.80 116.67 120.69 110.79 107.69 111.09 122.60 * * * * 167 HIS 167 1.314 1.241 1.514 1.556 1.449 120.13 115.86 120.55 111.17 110.83 112.75 123.59 * * * * 168 VAL 168 1.304 1.240 1.522 1.546 1.442 122.47 116.26 120.52 109.39 108.74 110.67 123.21 +* +* 169 LEU 169 1.301 1.237 1.524 1.567 1.445 122.28 115.88 120.50 111.97 108.28 109.55 123.59 ** +* * ** 170 ARG 170 1.313 1.240 1.517 1.540 1.446 123.33 116.94 120.25 110.34 108.70 111.23 122.81 * * 171 GLU 171 1.308 1.234 1.506 1.516 1.444 121.11 114.71 121.39 109.46 111.55 111.85 123.90 +* +* 172 ASP 172 1.301 1.244 1.509 1.545 1.446 123.12 116.38 120.16 109.37 108.83 110.70 123.45 ** ** 173 GLN 173 1.309 - 1.524 1.533 1.440 122.68 - - 110.53 109.02 111.40 - * * ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: *4.5* +* ** ** *** ** +* * +** ** ** * *4.5* ----------------------------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_5 Page 14 ---------------------------------------- A N A L Y S I S O F M A I N C H A I N B O N D L E N G T H S A N D B O N D A N G L E S +------------------+ | BOND LENGTHS | +------------------+ ------------------------------------------------------------------------------------------------------------- (Small molecule data) Number of Min Max Mean Standard Bond X-PLOR labelling Mean St. dev values value value value deviation ------------------------------------------------------------------------------------------------------------- C-N C-NH1 (except Pro) 1.329 .014 165 1.266 1.342 1.311 .013 *4.5* * C-N (Pro) 1.341 .016 7 1.335 1.346 1.339 .004 C-O C-O 1.231 .020 172 1.200 1.252 1.232 .008 +* * CA-C CH1E-C (except Gly) 1.525 .021 161 1.481 1.563 1.520 .014 ** +* CH2G*-C (Gly) 1.516 .018 12 1.491 1.533 1.508 .011 * CA-CB CH1E-CH3E (Ala) 1.521 .033 4 1.503 1.525 1.515 .008 CH1E-CH1E (Ile,Thr,Val) 1.540 .027 29 1.518 1.583 1.556 .015 +* CH1E-CH2E (the rest) 1.530 .020 128 1.490 1.577 1.535 .013 ** ** N-CA NH1-CH1E (except Gly,Pro)1.458 .019 154 1.393 1.491 1.447 .016 *** +* NH1-CH2G* (Gly) 1.451 .016 12 1.421 1.481 1.442 .017 +* +* N-CH1E (Pro) 1.466 .015 7 1.450 1.467 1.460 .007 * ------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_5 Page 15 ---------------------------------------- +-----------------+ | BOND ANGLES | +-----------------+ ------------------------------------------------------------------------------------------------------------- (Small molecule data) Number of Min Max Mean Standard Angle X-PLOR labelling Mean St. dev values value value value deviation ------------------------------------------------------------------------------------------------------------- CA-C-N CH1E-C-NH1 (except Gly,Pro)116.2 2.0 153 113.44 118.17 116.16 .99 * CH2G*-C-NH1 (Gly) 116.4 2.1 12 114.71 119.56 116.56 1.10 +* CH1E-C-N (Pro) 116.9 1.5 7 115.85 117.57 116.70 .57 O-C-N O-C-NH1 (except Pro) 123.0 1.6 165 121.23 124.66 123.04 .55 * * O-C-N (Pro) 122.0 1.4 7 121.60 123.19 122.64 .54 C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 154 119.20 126.19 122.15 1.21 * ** C-NH1-CH2G* (Gly) 120.6 1.7 11 118.89 124.20 121.04 1.52 * ** C-N-CH1E (Pro) 122.6 5.0 7 122.17 123.15 122.63 .27 CA-C-O CH1E-C-O (except Gly) 120.8 1.7 160 118.96 123.00 120.76 .62 * * CH2G*-C-O (Gly) 120.8 2.1 12 119.20 121.36 120.53 .57 CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 4 110.07 111.38 110.62 .48 CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 29 107.36 111.42 109.74 1.10 * CH2E-CH1E-C (the rest) 110.1 1.9 128 106.77 115.11 110.68 1.56 +* +** N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 154 104.40 115.25 110.23 1.72 ** * NH1-CH2G*-C (Gly) 112.5 2.9 12 108.32 119.55 112.18 2.69 * ** N-CH1E-C (Pro) 111.8 2.5 7 109.29 113.65 111.73 1.69 * N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 4 109.80 111.12 110.66 .52 NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 29 107.72 114.91 111.66 1.56 ** ** N-CH1E-CH2E (Pro) 103.0 1.1 7 101.81 103.74 103.30 .62 * NH1-CH1E-CH2E (the rest) 110.5 1.7 121 106.92 114.56 110.73 1.56 ** ** ------------------------------------------------------------------------------------------------------------- The small molecule data used in the above analysis is from Engh & Huber (1991). The atom labelling follows that used in the X-PLOR dictionary, with some additional atoms (marked with an asterisk) as defined by Engh & Huber. Residue-by-residue listing for refined_5 Page 16 ---------------------------------------- R A M A C H A N D R A N P L O T S T A T I S T I C S Residues in most favoured regions [A,B,L] 132 86.3% Residues in additional allowed regions [a,b,l,p] 17 11.1% Residues in generously allowed regions [~a,~b,~l,~p] 3 2.0% Residues in disallowed regions [XX] 1 .7% ---- ------ Number of non-glycine and non-proline residues 153 100.0% Number of end-residues (excl. Gly and Pro) 1 Number of glycine residues 12 Number of proline residues 7 ---- Total number of residues 173 Based on the analysis of 118 structures of resolution of at least 2.0 Angstroms and R-factor no greater than 20%, a good quality model would be expected to have over 90% in the most favoured regions [E,H,L]. S T E R E O C H E M I S T R Y O F M A I N - C H A I N Comparison values No. of No. of Parameter Typical Band band widths Stereochemical parameter data pts value value width from mean ------------------------ -------- ----- ----- ----- --------- a. %-tage residues in A, B, L 153 86.3 83.8 10.0 .2 Inside b. Omega angle st dev 172 3.7 6.0 3.0 -.8 Inside c. Bad contacts / 100 residues 0 .0 4.2 10.0 -.4 Inside d. Zeta angle st dev 161 2.0 3.1 1.6 -.7 Inside e. H-bond energy st dev 98 .9 .8 .2 .6 Inside f. Overall G-factor 173 .0 -.4 .3 1.3 BETTER S T E R E O C H E M I S T R Y O F S I D E - C H A I N Comparison values No. of No. of Parameter Typical Band band widths Stereochemical parameter data pts value value width from mean ------------------------ -------- ----- ----- ----- --------- a. Chi-1 gauche minus st dev 31 5.9 18.1 6.5 -1.9 BETTER b. Chi-1 trans st dev 58 8.5 19.0 5.3 -2.0 BETTER c. Chi-1 gauche plus st dev 61 7.1 17.5 4.9 -2.1 BETTER d. Chi-1 pooled st dev 150 8.7 18.2 4.8 -2.0 BETTER e. Chi-2 trans st dev 46 3.6 20.4 5.0 -3.4 BETTER M O R R I S E T A L . C L A S S I F I C A T I O N Mean St.dev Classification Parameter m s 1 2 3 4 Value Class --------- ---- --- ------------------------------------ ----- ----- Phi-psi distribution - - >75.0% >65.0% >55.0% <55.0% 86.3 1 Chi-1 st.dev. 18.2 6.2 <12.0 <18.2 <24.4 >24.4 8.9 1 H-bond energy st dev .87 .24 < .63 < .87 <1.11 >1.11 .94 3 Residue-by-residue listing for refined_5 Page 17 ---------------------------------------- G - F A C T O R S Average Parameter Score Score --------- ----- ----- Dihedral angles:- Phi-psi distribution -.46 Chi1-chi2 distribution -.21 Chi1 only -.20 Chi3 & chi4 .49 Omega .01 ------ -.12 ===== Main-chain covalent forces:- Main-chain bond lengths .05 Main-chain bond angles .41 ------ .25 ===== OVERALL AVERAGE .01 ===== Ideally, scores should be above -0.5. Values below -1.0 may need investigation.